A team led by Mary Estes of the Baylor College of Medicine used rotavirus as a model to study some of the proteins involved in making the cytoplasmic compartments in which many DNA and RNA virus pathogens replicate. Banumathi Sankaran, a research scientist in the Berkeley Center for Structural Biology (BSCB) at the Advanced Light Source, collected the X-ray data at the BCSB Beamline 5.0.1 that were used to solve the three-dimensional structures of nonstructural protein NSP2. Understanding the functions of proteins that make these compartments could offer an avenue for disrupting virus production. The team published their findings in Proceedings of the National Academy of Sciences.

Bioscientists at the Advanced Light Source (ALS) at Berkeley Lab lent their expertise to a project led by scientists at the University of Washington to design proteins in the lab that zip together like DNA. The technique could enable the design of protein nanomachines to help diagnose and treat disease, allow for more precise engineering of cells, and perform a variety of other tasks.

“Viruses are critical components of every microbial ecosystem. The JGI is especially interested in developing standards for virus genomes because we generate much of this data ourselves,” said JGI research scientist and first author Simon Roux.

As more and more researchers continue to assemble new genome sequences of uncultivated viruses, JGI researchers led a community effort to develop guidelines and best practices for defining virus data quality. In Nature Biotechnology, JGI partnered with a number of virus experts; as well as representatives from the Genomic Standards Consortium (GSC), an open-membership working body that engages the research community in the standards development process; and the International Committee on Taxonomy of Viruses, the premier authority on the official taxonomy of viruses which is currently re-evaluating virus classification based on sequence-based information.

An international team led by researchers at UCSF used protein crystallography at the Advanced Light Source (ALS) beamline 8.3.1 to obtain structures of several influenza antiviral drug molecules bound to their proton-channel targets in both open and closed conformations. These complexes provide the first high-resolution views of how the drugs interact with and disrupt the water-molecule networks lining the M2 transmembrane channel. The structures provide an atomic-level blueprint from which to design more effective anti-influenza drugs that can overcome growing drug resistance. ALS beamline 8.3.1 is operated by James Holton, MBIB beamline scientist and associate adjunct professor at UCSF.